Research Article

The modal distribution of protein isoelectric points reflects amino acid properties rather than sequence evolution

  1. Georg F. Weiller1,2,*,
  2. Gilles Caraux3,
  3. Nicole Sylvester2

Article first published online: 11 FEB 2004

DOI: 10.1002/pmic.200200648

Issue

PROTEOMICS

PROTEOMICS

Volume 4, Issue 4, pages 943–949, April 2004

Additional Information

How to Cite

Weiller, G. F., Caraux, G. and Sylvester, N. (2004), The modal distribution of protein isoelectric points reflects amino acid properties rather than sequence evolution. PROTEOMICS, 4: 943–949. doi: 10.1002/pmic.200200648

Author Information

  1. 1

    ARC Centre of Excellence for Integrative Legume Research, Australian National University, Canberra, Australia

  2. 2

    Research School of Biological Sciences, Australian National University, Canberra, Australia

  3. 3

    Département d'Informatique Fondamentale et Appliquée, LIRMM, Montpellier, France

*Bioinformatics Laboratory, Genomic Interactions Group, Research School of Biological Sciences, Australian National University, Canberra, ACT 0200, Australia Fax: +61-(0)-2-6125-9709

Publication History

  1. Issue published online: 23 MAR 2004
  2. Article first published online: 11 FEB 2004
  3. Manuscript Received: 19 DEC 2002

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Keywords:

  • Extremophiles;
  • Genome;
  • Isoelectric point;
  • Multimodal distribution

Abstract

Two-dimensional gel electrophoresis, a routine application in proteomics, separates proteins according to their molecular mass (Mr) and isoelectric point (pI). As the genomic sequences for more and more organisms are determined, the Mr and pI of all their proteins can be estimated computationally. The examination of several of these theoretical proteome plots has revealed a multimodal pI distribution, however, no conclusive explanation for this unusual distribution has so far been presented. We examined the pI distribution of 115 fully sequenced genomes and observed that the modal distribution does not reflect phylogeny or sequence evolution, but rather the chemical properties of amino acids. We provide a statistical explanation of why the observed distributions of pI values are multimodal.

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